ID   MTBA_ANEAE              Reviewed;         428 AA.
AC   P19888;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   08-NOV-2023, entry version 98.
DE   RecName: Full=Type II methyltransferase M.BanI {ECO:0000303|PubMed:12654995};
DE            Short=M.BanI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase BanI;
DE   AltName: Full=Modification methylase BanI;
GN   Name=banIM;
OS   Aneurinibacillus aneurinilyticus (Bacillus aneurinolyticus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 12856 / DSM 5562 / JCM 9024 / NBRC 15521 / IAM 1077 / NRS
RC   1589;
RX   PubMed=2358438; DOI=10.1093/oxfordjournals.jbchem.a123101;
RA   Maekawa Y., Yasukawa H., Kawakami B.;
RT   "Cloning and nucleotide sequences of the BanI restriction-modification
RT   genes in Bacillus aneurinolyticus.";
RL   J. Biochem. 107:645-649(1990).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A methylase, recognizes the double-stranded sequence 5'-
CC       GGYRCC-3', methylates C-4 on both strands, and protects the DNA from
CC       cleavage by the BanI endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:2358438}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2358438}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; D00704; BAA00613.1; -; Genomic_DNA.
DR   PIR; JS0489; CTBSBA.
DR   RefSeq; WP_021624992.1; NZ_CABKST010000283.1.
DR   AlphaFoldDB; P19888; -.
DR   SMR; P19888; -.
DR   OrthoDB; 9813719at2; -.
DR   PRO; PR:P19888; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..428
FT                   /note="Type II methyltransferase M.BanI"
FT                   /id="PRO_0000087860"
FT   DOMAIN          3..417
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   428 AA;  48618 MW;  ADF3E932A681E43E CRC64;
     MKIKFVDLFA GIGGIRIGFE RAAKRFELET ECVLSSEIDK KACETYALNF KEEPQGDIHE
     ITSFPEFDFL LAGFPCQPFS YAGKQQGFGD TRGTLFFEVE RVLRDNRPKA FLLENVRGLV
     THDKGRTLKT IISKLEELGY GVSYLLLNSS TFGVPQNRVR IYILGILGSK PKLTLTSNVG
     AADSHKYKNE QISLFDESYA TVKDILEDSP SEKYRCSDEF IGQLSKVVGN NFELLHGYRL
     IDYRGGNSIH SWELGIKGDC TKEEIEFLNQ LIANRRKKIY GTHQDGKALT LEQIRTFYNH
     DQLEVIIKSL LQKGYLREEE NKFNPVCGNM SFEVFKFLDP DSISITLTSS DAHKLGVVQN
     NVPRRITPRE CARLQGFPDD FILHSNDNFA YKQLGNSVTV KVVEKVIEDL FQNNVNELFG
     QMKLANVV
//